Hyaluronic acid binding to CD44S is indiscriminate of molecular weight

Two methods for the preparation of high molecular weight [3H]hyaluronic acid were investigated. In the first one, hydrogen atoms in the molecule were replaced by tritium. This isotopic substitution was performed in aqueous solution using Pd/CaCO3 as the catalyst. In the second method, the high molecular weight hyaluronic acid was alkylated with [3H]methyl bromide in liquid ammonia at a temperature of -33.5 °C. High-performance gel permeation chromatographic separation method was used for the isolation and characterization of the high molecular weight [3H]hyaluronic acid. Molecular weight parameters for the labelled biopolymers were Mw = 128 kDa, Mw/Mn = 1.88 (first method) and Mw = 268 kDa, Mw/Mn = 1.55 (second method). The high molecular weight [3H]hyaluronic acid having Mw = 268 kDa was degraded further by specific hyaluronidase. Products of the enzymatic depolymerization were observed to be identical for both, labelled and cold biopolymer. This finding indicates that the described labelling procedure using [3H]methyl bromide does not induce any major structural rearrangements in the molecule.

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High molecular weight form of hyaluronic acid reduces neuroinflammatory response in injured sciatic nerve via the intracellular domain of CD44

Journal of Biomedical Materials Research Part B Applied Biomaterials ◽

10.1002/jbm.b.34731 ◽

2020 ◽

Vol 109 (5) ◽

pp. 673-680

Author(s):

I‐Ming Jou ◽

Tung‐Tai Wu ◽

Che‐Chia Hsu ◽

Cheng‐Chang Yang ◽

Jhy‐Shrian Huang ◽

...

Keyword(s):

Molecular Weight ◽

Hyaluronic Acid ◽

Sciatic Nerve ◽

High Molecular Weight ◽

Intracellular Domain ◽

Neuroinflammatory Response ◽

High Molecular Weight Form ◽

Molecular Weight Form

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Wound Healing Promotion by Hyaluronic Acid: Effect of Molecular Weight on Gene Expression and In Vivo Wound Closure

Pharmaceuticals ◽

10.3390/ph14040301 ◽

2021 ◽

Vol 14 (4) ◽

pp. 301

Author(s):

Yayoi Kawano ◽

Viorica Patrulea ◽

Emmanuelle Sublet ◽

Gerrit Borchard ◽

Takuya Iyoda ◽

...

Keyword(s):

Gene Expression ◽

Molecular Weight ◽

Wound Healing ◽

Hyaluronic Acid ◽

Healing Process ◽

Dermal Fibroblasts ◽

Water Soluble ◽

Wound Healing Process ◽

And Migration ◽

Proliferation And Migration

Hyaluronic acid (HA) has been known to play an important role in wound healing process. However, the effect of molecular weight (MW) of exogenously administered HA on the wound healing process has not been fully understood. In this study, we investigated HA with different MWs on wound healing process using human epidermal keratinocytes and dermal fibroblasts. Cell proliferation and migration ability were assessed by water soluble tetrazolium (WST) assay and wound scratch assay. We examined the effect of HA addition in a full-thickness wound model in mice and the gene expression related to wound healing. Proliferation and migration of HaCaT cells increased with the increase of MW and concentration of HA. Interleukin (IL-1β), IL-8 and vascular endothelial growth factor (VEGF) as well as matrix metalloproteinase (MMP)-9 and MMP-13 were significantly upregulated by high molecular weight (HMW) HA in keratinocytes. Together with VEGF upregulation and the observed promotion of HaCaT migration, HA with the MW of 2290 kDa may hold potential to improve re-epithelialization, a critical obstacle to heal chronic wounds.

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Successful outcomes of a novel endoscopic treatment for GI tumors: endoscopic submucosal dissection with a mixture of high-molecular-weight hyaluronic acid, glycerin, and sugar

Gastrointestinal Endoscopy ◽

10.1016/j.gie.2005.08.002 ◽

2006 ◽

Vol 63 (2) ◽

pp. 243-249 ◽

Cited By ~ 174

Author(s):

Mitsuhiro Fujishiro ◽

Naohisa Yahagi ◽

Masanori Nakamura ◽

Naomi Kakushima ◽

Shinya Kodashima ◽

...

Keyword(s):

Molecular Weight ◽

Hyaluronic Acid ◽

Endoscopic Submucosal Dissection ◽

High Molecular Weight ◽

Endoscopic Treatment ◽

Submucosal Dissection ◽

Successful Outcomes

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Sperm concentration, hyaluronic acid-binding capacity, aneuploidy and persistent histones in testicular cancer

Human Reproduction ◽

10.1093/humrep/deu179 ◽

2014 ◽

Vol 29 (9) ◽

pp. 1866-1874 ◽

Cited By ~ 7

Author(s):

Z. Molnar ◽

A. Mokanszki ◽

Z. Kassai Bazsane ◽

H. P. Bhattoa ◽

M. Benyo ◽

...

Keyword(s):

Hyaluronic Acid ◽

Testicular Cancer ◽

Binding Capacity ◽

Sperm Concentration ◽

Hyaluronic Acid Binding

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Immunochemical analysis of cartilage proteoglycans. Radioimmunoassay of the molecules and the substructures

Biochemical Journal ◽

10.1042/bj1870687 ◽

1980 ◽

Vol 187 (3) ◽

pp. 687-694 ◽

Cited By ~ 19

Author(s):

J Wieslander ◽

D Heinegárd

Keyword(s):

Hyaluronic Acid ◽

Uronic Acid ◽

Chondroitin Sulphate ◽

Relative Content ◽

Binding Region ◽

Rich Region ◽

Link Protein ◽

Specific Radioimmunoassay ◽

Cartilage Proteoglycans ◽

Hyaluronic Acid Binding

Antibodies specifically reacting with the link proteins, the hyaluronic acid-binding region and chondroitin sulphate-peptides were used to design specific radioimmunoassay procedures. The sensitivity of the method used for the link protein was about 20 ng/ml, and the other two components could be determined at concentrations of about 2 ng/ml. The radioimmunoassay procedures were tested by using proteoglycan subfractions or fragments thereof. The procedures used to quantify link protein and hyaluronic acid-binding region showed no cross-interference. Fragments of trypsin-digested proteoglycan monomers still reacted in the radioimmunoassay for hyaluronic acid-binding region. Subfractions of proteoglycan monomers separated according to size had a gradually higher relative content of the hyaluronic acid-binding region compared with both chondroitin sulphate-peptides and uronic acid, when the molecules were smaller. The proteoglycans therefore may contain a variably large chondroitin sulphate-rich region, which has a constant substitution with polysaccharide side chains.

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The properties of proteoglycan prepared from human articular cartilage by using associative caesium chloride gradients of high and low starting densities

Biochemical Journal ◽

10.1042/bj2320111 ◽

1985 ◽

Vol 232 (1) ◽

pp. 111-117 ◽

Cited By ~ 25

Author(s):

M T Bayliss ◽

P J Roughley

Keyword(s):

Hyaluronic Acid ◽

Articular Cartilage ◽

Proteinase Inhibitors ◽

Density Gradient Centrifugation ◽

Gradient Centrifugation ◽

Human Articular Cartilage ◽

Adult Human ◽

Cscl Density Gradient ◽

Proteoglycan Aggregates ◽

Hyaluronic Acid Binding

Proteoglycan was extracted from adult human articular cartilage from both the knee and the hip, and A1 preparations were prepared by CsCl-density-gradient centrifugation at starting densities of 1.69 and 1.5 g/ml. Irrespective of whether the cartilage was diced to 1 mm cubes or sectioned to 20 micron slices there was always a lower proportion of both protein and proteoglycan aggregate in the A1 preparation prepared at 1.69 g/ml. Furthermore, the addition of exogenous hyaluronic acid to the extracts before centrifugation did not improve the yield of aggregate at 1.69 g/ml. These results were not affected by the presence of proteinase inhibitors in the extraction medium. It appears that adult human articular cartilage contains a high proportion of low-density proteoglycan subunits and hyaluronic acid-binding proteins that make most of the re-formed proteoglycan aggregates of a lower density than is usually encountered with younger human and mammalian hyaline cartilages.

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